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Protein

Glutamine synthetase

Gene

glnA

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.1 Publication

Miscellaneous

GlnA of S.acidocaldarius is unique among the archeal glutamine synthetase since the regulatory properties suggest a position within the GS I-alpha subgroup. However, the sequence shows more pronounced similarities to the GS I-beta subgroup.1 Publication

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 Mg2+ or Mn2+ ions per subunit.By similarity

Enzyme regulationi

Strongly inhibited by glycine and L-alanine. AMP at 10 mM displays a very weak inhibitory effect. The activity of this enzyme is not controlled by adenylation.1 Publication

Kineticsi

  1. KM=0.15 mM for ADP1 Publication
  2. KM=0.24 mM for manganese1 Publication
  3. KM=1.3 mM for L-glutamine1 Publication

    pH dependencei

    Optimum pH is between 7 and 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius. In the absence of magnesium or manganese ions about 50% of the activity is lost within 100 minutes at 78 degrees Celsius, whereas more than 95% of the activity is retained in presence of 4 mM manganese ions. Magnesium ions are a less effective.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi133Magnesium 1By similarity1
    Metal bindingi135Magnesium 2By similarity1
    Binding sitei207ATPBy similarity1
    Metal bindingi212Magnesium 2By similarity1
    Metal bindingi220Magnesium 2By similarity1
    Binding sitei265L-glutamate; via carbonyl oxygenBy similarity1
    Metal bindingi269Magnesium 1; via pros nitrogenBy similarity1
    Binding sitei273ATPBy similarity1
    Binding sitei324L-glutamateBy similarity1
    Binding sitei330L-glutamateBy similarity1
    Binding sitei342ATPBy similarity1
    Binding sitei342L-glutamateBy similarity1
    Binding sitei347ATPBy similarity1
    Binding sitei357ATPBy similarity1
    Metal bindingi362Magnesium 1By similarity1
    Binding sitei364L-glutamateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi271 – 273ATPBy similarity3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLigase
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.1.2 6160

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase1 Publication (EC:6.3.1.21 Publication)
    Short name:
    GS1 Publication
    Alternative name(s):
    Glutamate--ammonia ligaseCurated
    Glutamine synthetase I alphaCurated
    Short name:
    GSI alphaCurated
    Gene namesi
    Name:glnA1 Publication
    Ordered Locus Names:Saci_1483
    OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
    Taxonomic identifieri330779 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001018 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001532132 – 473Glutamine synthetaseAdd BLAST472

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9HH09

    Interactioni

    Subunit structurei

    Oligomer of 12 subunits arranged in the form of two hexagons.1 Publication

    Protein-protein interaction databases

    STRINGi330779.Saci_1483

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HH09
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni264 – 265L-glutamate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiarCOG01909 Archaea
    COG0174 LUCA
    HOGENOMiHOG000005157
    KOiK01915
    OMAiVFPWESK
    OrthoDBiPOG093Z00GE

    Family and domain databases

    Gene3Di3.10.20.70, 1 hit
    InterProiView protein in InterPro
    IPR008147 Gln_synt_b-grasp
    IPR036651 Gln_synt_N
    IPR014746 Gln_synth/guanido_kin_cat_dom
    IPR008146 Gln_synth_cat_dom
    IPR027303 Gln_synth_gly_rich_site
    IPR004809 Gln_synth_I
    IPR027302 Gln_synth_N_conserv_site
    PfamiView protein in Pfam
    PF00120 Gln-synt_C, 1 hit
    PF03951 Gln-synt_N, 1 hit
    SMARTiView protein in SMART
    SM01230 Gln-synt_C, 1 hit
    SUPFAMiSSF54368 SSF54368, 1 hit
    SSF55931 SSF55931, 1 hit
    TIGRFAMsiTIGR00653 GlnA, 1 hit
    PROSITEiView protein in PROSITE
    PS00180 GLNA_1, 1 hit
    PS00181 GLNA_ATP, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9HH09-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPGLPKNEHE ALEFLKSNNI KWVDLQFTDL LGKLQHITIP SNEFDESSFK
    60 70 80 90 100
    VGFGKLDGSS IKGFTSIYES DMVLLPIPQT MTLIPWMQGV ARVLTKVFWG
    110 120 130 140 150
    GGKGRFERDP RGIAEEAEKY QSEQGYVSYF GPELEFFVFD KVEVDASLPQ
    160 170 180 190 200
    SGTGYKIHSR EAPWSKNGGY VIRYKEGYYP ASPVDQLMDI RLEIISTLVD
    210 220 230 240 250
    YFGFTIEAAH HEVATAGQGE IDFRFSTLAD TADKVQVLKY VTKNIASKRG
    260 270 280 290 300
    MIATFMPKPF FGDNGSGMHT HFSLWTKDGK NLMYDPNDEY AELSQIGRYI
    310 320 330 340 350
    IGGLLEHGRA LSAIVAPTTN SYRRLVPGYE APVYLVWSKS NRSAAIRIPA
    360 370 380 390 400
    YYKGMEKAKR LEYRPPDPSS NPYLVFSAIL MAGLDGIRRK LDPGDPVDEN
    410 420 430 440 450
    IYHMSEEKKR SLKIRELPGS LDEALNELES DNEFLKPVFN SSILQAYLDL
    460 470
    KKEEAKMMQL YPHPMEIYQY LDS
    Length:473
    Mass (Da):53,586
    Last modified:August 30, 2005 - v2
    Checksum:iF8EA4FD71B1CDD5D
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti185D → V in CAC20905 (PubMed:9865608).Curated1
    Sequence conflicti204 – 207FTIE → TIEA in CAC20905 (PubMed:9865608).Curated4
    Sequence conflicti209A → H in CAC20905 (PubMed:9865608).Curated1
    Sequence conflicti211 – 259HEVAT…FMPKP → EVATAGQGDIDFRFSTLADT ADKVQVLKYVTKNIASKRGM IATFMPKPF in CAC20905 (PubMed:9865608).CuratedAdd BLAST49
    Sequence conflicti261 – 299FGDNG…QIGRY → GDNGSGMHTHFSLWTKDGKN LMYDPNDEYAELSQIGRYI in CAC20905 (PubMed:9865608).CuratedAdd BLAST39
    Sequence conflicti301 – 303IGG → GPL in CAC20905 (PubMed:9865608).Curated3
    Sequence conflicti305 – 314LEHGRALSAI → EHGRALSAIV in CAC20905 (PubMed:9865608).Curated10
    Sequence conflicti317P → G in CAC20905 (PubMed:9865608).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ224678 Genomic DNA Translation: CAC20905.1
    CP000077 Genomic DNA Translation: AAY80804.1
    RefSeqiWP_011278306.1, NC_007181.1

    Genome annotation databases

    EnsemblBacteriaiAAY80804; AAY80804; Saci_1483
    GeneIDi3474677
    KEGGisai:Saci_1483
    PATRICifig|330779.12.peg.1427

    Similar proteinsi

    Entry informationi

    Entry nameiGLN1A_SULAC
    AccessioniPrimary (citable) accession number: Q9HH09
    Secondary accession number(s): Q4J8S1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: August 30, 2005
    Last modified: May 23, 2018
    This is version 98 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

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